Localization, Extraction, and Quantification of Plant and Algal Arabinogalactan Proteins

Veenhof, Reina J.; Popper, Zoë A.

doi:10.1007/978-1-0716-0621-6_24

Cited by 3 publications

(2 citation statements)

References 55 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The amount of AGPs in 1.5 mg of dry weight sample was quantified in accordance with the protocol described by Lamport (2013) via a gum arabic standard. β‐Yariv gel diffusion and electrophoresis was performed as described by Veenhof & Popper (2020). Briefly, soluble AGPs were extracted by adding 50 μl of demineralized water per mg of dry weight.…”

Section: Methodsmentioning

confidence: 99%

CAGEs are Golgi‐localized GT31 enzymes involved in cellulose biosynthesis in Arabidopsis

et al. 2022

View full text Add to dashboard Cite

SUMMARY Cellulose is the main structural component in the plant cell walls. We show that two glycosyltransferase family 31 (GT31) enzymes of Arabidopsis thaliana, here named cellulose synthesis associated glycosyltransferases 1 and 2 (CAGE1 and 2), influence both primary and secondary cell wall cellulose biosynthesis. cage1cage2 mutants show primary cell wall defects manifesting as impaired growth and cell expansion in seedlings and etiolated hypocotyls, along with secondary cell wall defects, apparent as collapsed xylem vessels and reduced xylem wall thickness in the inflorescence stem. Single and double cage mutants also show increased sensitivity to the cellulose biosynthesis inhibitor isoxaben. The cage1cage2 phenotypes were associated with an approximately 30% reduction in cellulose content, an approximately 50% reduction in secondary cell wall CELLULOSE SYNTHASE (CESA) protein levels in stems and reduced cellulose biosynthesis rate in seedlings. CESA transcript levels were not significantly altered in cage1cage2 mutants, suggesting that the reduction in CESA levels was caused by a post‐transcriptional mechanism. Both CAGE1 and 2 localize to the Golgi apparatus and are predicted to synthesize β‐1,3‐galactans on arabinogalactan proteins. In line with this, the cage1cage2 mutants exhibit reduced levels of β‐Yariv binding to arabinogalactan protein linked β‐1,3‐galactan. This leads us to hypothesize that defects in arabinogalactan biosynthesis underlie the cellulose deficiency of the mutants.

show abstract

Section: Methodsmentioning

confidence: 99%

CAGEs are Golgi‐localized GT31 enzymes involved in cellulose biosynthesis in Arabidopsis

et al. 2022

View full text Add to dashboard Cite

show abstract

“…The amount of AGPs in 1.5 mg of dry weight sample was quantified according to the protocol described by Lamport (2013) via a gum Arabic standard. The β-yariv gel diffusion and electrophoresis was performed according to the protocol described by Veenhof and Popper (2020). Briefly, soluble AGPs were extracted by adding 50 µl demineralized water per mg of dry weight.…”

Section: Agp Analysis Using β-Yariv Precipitationmentioning

confidence: 99%

Golgi-localized GALT7 and GALT8 participate in cellulose biosynthesis

Nibbering

Castilleux

Wingsle

et al. 2021

Preprint

View full text Add to dashboard Cite

Arabinogalactan protein (AGP) glycan biosynthesis in the Golgi apparatus contributes to plant cell wall assembly, but the mechanisms underlying this process are largely unknown. Here, we show that two putative galactosyltransferases -named GALT7 and GALT8 -from the glycosyltransferase family 31 (GT31) of Arabidopsis thaliana participate in cellulose biosynthesis. galt7galt8 mutants show primary cell wall defects manifesting as impaired growth and cell expansion in seedlings and etiolated hypocotyls, along with secondary cell wall defects, apparent as collapsed xylem vessels and reduced xylem wall thickness in the inflorescence stem. These phenotypes were associated with a ∼30% reduction in cellulose content, a ∼50% reduction in secondary cell wall CELLULOSE SYNTHASE (CESA) protein levels and reduced cellulose biosynthesis rate. CESA transcript levels were not significantly altered in galt7galt8 mutants, suggesting that the reduction in CESA levels was caused by a post-transcriptional mechanism. We provide evidence that both GALT7 and GALT8 localise to the Golgi apparatus, while quantitative proteomics experiments revealed reduced levels of the entire FLA subgroup B in the galt7galt8 mutants. This leads us to hypothesize that a defect in FLA subgroup B glycan biosynthesis reduces cellulose biosynthesis rate in galt7galt8 mutants.

show abstract

Applications of the Yariv reagent in polysaccharide analysis and plant physiology from theory to practice

Chen,

et al. 2024

Carbohydrate Polymers

View full text Add to dashboard Cite

Localization, Extraction, and Quantification of Plant and Algal Arabinogalactan Proteins

Cited by 3 publications

References 55 publications

CAGEs are Golgi‐localized GT31 enzymes involved in cellulose biosynthesis in Arabidopsis

CAGEs are Golgi‐localized GT31 enzymes involved in cellulose biosynthesis in Arabidopsis

Golgi-localized GALT7 and GALT8 participate in cellulose biosynthesis

Applications of the Yariv reagent in polysaccharide analysis and plant physiology from theory to practice

Contact Info

Product

Resources

About